Zegerman, P., Canas, B., Pappin, D., Kouzarides, T. (April 2002) Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem, 277 (14). pp. 11621-4. ISSN 0021-9258 (Print)0021-9258 (Linking)
Abstract
Histone N-terminal tails are post-translationally modified in many ways. At lysine residues, histones can be either acetylated or methylated. Both modifications lead to the binding of specific proteins; bromodomain proteins, such as GCN5, bind acetyl lysines and the chromodomain protein, HP1, binds methyl lysine 9 of histone H3. Here we show that the previously characterized transcriptional repressor complex NuRD (nucleosome remodeling and deacetylase) binds to the histone H3 N-terminal tail and that methylation at lysine 4, but not lysine 9, prevents binding. Given that lysine 4 methylation is found at sites of active transcription, these results suggest that a function of lysine 4 methylation is to disrupt the association of histones with a repressor complex.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Acetylation Blotting, Western Cell Nucleus/metabolism Electrophoresis, Polyacrylamide Gel HeLa Cells Histone Deacetylases/ chemistry/ metabolism Histones/ chemistry/ metabolism Humans Lysine/ chemistry Mass Spectrometry Methylation Mi-2 Nucleosome Remodeling and Deacetylase Complex Peptides/chemistry Precipitin Tests Protein Binding Protein Structure, Tertiary Transcription, Genetic |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > nucleosome bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > post-translational modification |
| CSHL Authors: | |
| Communities: | CSHL labs > Pappin lab |
| Depositing User: | Matt Covey |
| Date: | 5 April 2002 |
| Date Deposited: | 17 Sep 2014 16:53 |
| Last Modified: | 17 Sep 2014 16:53 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/30756 |
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